1. The 1.7 Å crystal structure of the C5a peptidase from Streptococcus agalactiae (ScpB) reveals an active site competent for catalysis.
- Author
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Cullen R, Teçza M, Miclot T, Behan S, Jain M, Avink MK, Cooney JC, and Kagawa TF
- Subjects
- Humans, Catalytic Domain, Adhesins, Bacterial chemistry, Adhesins, Bacterial metabolism, Catalysis, Streptococcus pyogenes, Streptococcus agalactiae metabolism, Endopeptidases chemistry
- Abstract
A 1.7 Å structure is presented for an active form of the virulence factor ScpB, the C5a peptidase from Streptococcus agalactiae. The previously reported structure of the ScpB active site mutant exhibited a large separation (~20 Å) between the catalytic His and Ser residues. Significant differences are observed in the catalytic domain between the current and mutant ScpB structures resulting with a high RMSD
Cα (4.6 Å). The fold of the active form of ScpB is nearly identical to ScpA (RMSDCα 0.2 Å), the C5a-peptidase from Streptococcus pyogenes. Both ScpA and ScpB have comparable activity against human C5a, indicating neither enzyme require host proteins for C5a-ase activity. These studies are a first step in resolving reported differences in the specificities of these enzymes., (© 2023 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals LLC.)- Published
- 2024
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